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The results suggest that the Arctic populations of East Siberia are characterised by specificity of genetic make-up responsible for the activity of L-ficolin.
study provides evidence for an important role for the lectin pathway in the inflammatory response induced by cholesterol crystals (CC) and emphasize the role of ficolin-2 and MBL in the CC-mediated inflammation occurring during atherosclerotic plaque development
FCN2 inhibits epithelial-mesenchymal transition-induced metastasis of hepatocellular carcinoma via TGF-beta1 (show TGFB1 Proteins)/Smad (show SMAD1 Proteins) signaling.
this study shows that FCN2 polymorphisms is not a major risk factor for community-acquired pneumonia in general, but that the +6424G>T SNP in the FCN2 gene predisposes to Coxiella burnetii pneumonia
subjects that were heterozygote carriers of both FCN2 + 6424 and FCN3 (show FCN3 Proteins) + 1637delC were sufficient mannan-binding lectin (show MBL2 Proteins) producers
systemic lupus erythematosus patients with low plasma ficolin-2 levels had an increased risk of having lupus nephritis
Ficolin-2 protein could bind with HIV-1 envelope glycoprotein (show ERVW-1 Proteins) gp120 (show ITIH4 Proteins), and subsequently induce complement dependent cytotoxicity.
The FCN2 c.772G>T genotype appears to be associated with predisposition to chronic adenotonsillitis in the pediatric age group.
Serum levels of ficolin-2 and ficolin-3 (show FCN3 Proteins) were significantly lower in the cardiac syndrome X patients compared to controls.
association of FCN2 polymorphisms with nephritis and severe cumulative damage in SLE patients; no association with rheumatoid arthritis development
Ficolin-2 defends against virulent Mycobacteria tuberculosis infection in vivo, and its insufficiency is associated with infection in humans.
Data show that ficolin-B is stored in and set free from immature granulocytic myeloid cells indicating a role in the early infection-induced cellular response of these inflammatory cells.
FcnA-deficient and FcnA/ficolin B double-deficient mice lack FcnA-mediated complement activation in the sera, because of absence of complexes comprising FcnA and MBL-associated serine proteases.
These results identify mouse ficolin-B as a functional member of the ficolin family activating complement via the lectin pathway.
Results show that ficolin B in mouse bone marrow is an oligomeric protein. Ficolin B contained very low, but detectable, amounts of MASP-2 and sMAP and showed detectable C4-deposition activity on immobilized N-acetylglucosamine.
Ficolin B exhibited a distinct ontogeny pattern that switched from embryonic liver to postnatal bone marrow and spleen. The cells that express ficolin B mRNA were identified as belonging to the myeloid cell lineage.
Ficolin B showed multimeric structures and revealed binding to both N-acetylglucosamine and N-acetylgalactosamine. Ficolin B specifically recognized sialic acid residues. Ficolin B plays a distinct role through its unique carbohydrate-binding specificity.
The product of this gene belongs to the ficolin family of proteins. This family is characterized by the presence of a leader peptide, a short N-terminal segment, followed by a collagen-like region, and a C-terminal fibrinogen-like domain. This gene is predominantly expressed in the liver, and has been shown to have carbohydrate binding and opsonic activities. Alternatively spliced transcript variants encoding different isoforms have been identified.
ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)
, ficolin 2
, 37 kDa elastin-binding protein
, collagen/fibrinogen domain-containing protein 2
, ficolin B
, serum lectin p35